AC   MF_00553;
DC   Protein; auto
TR   HAMAP; MF_00553; -; 1; level=0
XX
Names: PAN
XX
ID   PAN
DE   RecName: Full=Proteasome-activating nucleotidase;
DE            Short=PAN;
DE            EC=3.6.1.-;
DE   AltName: Full=Proteasomal ATPase;
DE   AltName: Full=Proteasome regulatory ATPase;
DE   AltName: Full=Proteasome regulatory particle;
GN   Name=pan;
XX
CC   -!- FUNCTION: ATPase which is responsible for recognizing, binding,
CC       unfolding and translocation of substrate proteins into the archaeal 20S
CC       proteasome core particle. Is essential for opening the gate of the 20S
CC       proteasome via an interaction with its C-terminus, thereby allowing
CC       substrate entry and access to the site of proteolysis. Thus, the C-
CC       termini of the proteasomal ATPase function like a 'key in a lock' to
CC       induce gate opening and therefore regulate proteolysis. Unfolding
CC       activity requires energy from ATP hydrolysis, whereas ATP binding alone
CC       promotes ATPase-20S proteasome association which triggers gate opening,
CC       and supports translocation of unfolded substrates.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC   -!- SUBUNIT: Homohexamer. The hexameric complex has a two-ring architecture
CC       resembling a top hat that caps the 20S proteasome core at one or both
CC       ends. Upon ATP-binding, the C-terminus of PAN interacts with the alpha-
CC       rings of the proteasome core by binding to the intersubunit pockets.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DOMAIN: Consists of three main regions, an N-terminal coiled-coil
CC       domain that may assist in substrate recognition, an interdomain
CC       involved in PAN hexamerization, and a C-terminal ATPase domain of the
CC       AAA type.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
XX
DR   PROSITE; PS00674; AAA; 1; trigger=no
DR   Pfam; PF00004; AAA; 1; trigger=no
DR   NCBIfam; TIGR01242; 26Sp45; 1; trigger=no
DR   General; Coiled_coil; -; 0-unlimited; trigger=yes
XX
KW   Chaperone
KW   Cytoplasm
KW   Proteasome
KW   ATP-binding
KW   Nucleotide-binding
KW   Hydrolase
XX
GO   GO:0005524; F:ATP binding
GO   GO:0016887; F:ATP hydrolysis activity
GO   GO:0010498; P:proteasomal protein catabolic process
GO   GO:0043335; P:protein unfolding
GO   GO:0000502; C:proteasome complex
GO   GO:0005737; C:cytoplasm
GO   GO:0022623; C:proteasome-activating nucleotidase complex
XX
FT   From: PAN_PYRFU (Q8U4H3)
FT   REGION          394..396
FT                   /note="Docks into pockets in the proteasome alpha-ring to
FT                   cause gate opening"
FT   Condition: x-[YF]-x
FT   BINDING         140
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G
FT   BINDING         181
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G
FT   BINDING         182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: C
FT   BINDING         183
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G
FT   BINDING         184
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: K
FT   BINDING         185
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: T
FT   BINDING         186
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: L
XX
Size: 392-436;
Related: None;
Template: Q58576; O28303; D4GUJ7; Q5UT56; Q8U4H3;
Scope:
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in HALSA, HALVD
Plasmid: None
Comments: The protein performing the same function in bacteria (called ARC) is in MF_02112.
XX
# Version: 23
# Last updated date: 2025-06-20
# Created date: 2005-02-28
//